Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: Implications for allosteric regulation
A central problem in understanding enzyme regulation is to define the conformational states that account for allosteric changes in catalytic activity. For Escherichia coli aspartate transcarbamoylase (ATCase; EC 2.1.3.2) the active, relaxed (R state) holoenzyme is generally assumed to be represented...
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| Publicado no: | Proc Natl Acad Sci U S A |
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| Principais autores: | , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
National Academy of Sciences
2000
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC25784/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10805770/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.090087197 |
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